STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
glySKEGG: yps:YPTB3916 glycyl-tRNA synthetase beta subunit. (700 aa)    
Predicted Functional Partners:
glyQ
PFAM: glycyl-tRNA synthetase, alpha subunit; KEGG: pca:Pcar_0598 glycyl-tRNA synthetase, alpha subunit.
 0.999
leuS
TIGRFAM: leucyl-tRNA synthetase; KEGG: pca:Pcar_1413 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
   
  
 0.826
ileS
Isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.
 
  
 0.809
ybeY
Protein of unknown function UPF0054; Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
 
     0.805
lnt
Apolipoprotein N-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation; Belongs to the CN hydrolase family. Apolipoprotein N- acyltransferase subfamily.
       0.778
valS
valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
  
  
 0.770
Mmc1_1437
KEGG: pca:Pcar_1232 HD domain protein; TIGRFAM: metal dependent phophohydrolase; PFAM: metal-dependent phosphohydrolase, HD sub domain; metal-dependent phosphohydrolase, 7TM intracellular region; SMART: metal-dependent phosphohydrolase, HD region.
       0.750
alaS
alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
 
  
 0.701
aspS
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
  
 0.693
pheT
TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: pca:Pcar_1423 phenylalanyl-tRNA synthetase, beta subunit.
  
  
 0.667
Your Current Organism:
Magnetococcus marinus
NCBI taxonomy Id: 156889
Other names: M. marinus MC-1, Magnetococcus marinus MC-1, Magnetococcus marinus str. MC-1, Magnetococcus marinus strain MC-1, Magnetococcus sp. MC-1
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